3oob

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:35, 21 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3oob' size='340' side='right'caption='[[3oob]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
<StructureSection load='3oob' size='340' side='right'caption='[[3oob]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3oob]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OOB FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3oob]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OOB FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KDH:(2R,3R)-5,7-DIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-3,4-DIHYDRO-2H-CHROMEN-3-YL+3,4,5-TRIHYDROXYBENZOATE'>KDH</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2itk|2itk]], [[2q5a|2q5a]], [[1f8a|1f8a]], [[1pin|1pin]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KDH:(2R,3R)-5,7-DIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-3,4-DIHYDRO-2H-CHROMEN-3-YL+3,4,5-TRIHYDROXYBENZOATE'>KDH</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIN1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oob OCA], [https://pdbe.org/3oob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oob RCSB], [https://www.ebi.ac.uk/pdbsum/3oob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oob ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oob OCA], [https://pdbe.org/3oob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oob RCSB], [https://www.ebi.ac.uk/pdbsum/3oob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oob ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN]] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>
+
[https://www.uniprot.org/uniprot/PIN1_HUMAN PIN1_HUMAN] Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation.<ref>PMID:15664191</ref> <ref>PMID:16644721</ref> <ref>PMID:21497122</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The most active anticancer component in green tea is epigallocatechin-3-gallate (EGCG). The human peptidyl prolyl cis/trans isomerase (Pin1) plays a critical role in oncogenic signaling. Herein, we report the X-ray crystal structure of the Pin1/EGCG complex resolved at 1.9 A resolution. Notably, the structure revealed the presence of EGCG in both the WW and PPIase domains of Pin1. The direct binding of EGCG with Pin1 was confirmed and the interaction inhibited Pin1 PPlase activity. In addition, proliferation of cells expressing Pin1 was inhibited and tumor growth in a xenograft mouse model was suppressed. The binding of EGCG with Arg17 in the WW domain prevented the binding of c-Jun, a well-known Pin1 substrate. EGCG treatment corresponded with a decreased abundance of cyclin D1 and diminution of TPA-induced AP-1 or NFkappaB promoter activity in cells expressing Pin1. Overall, these results showed that EGCG directly suppresses the tumor promoting effect of Pin1.
+
-
 
+
-
Epigallocatechin-gallate suppresses tumorigenesis by directly targeting Pin1.,Urusova D, Shim J, Kim DJ, Jung SK, Zykova T, Carper A, Bode AM, Dong Z Cancer Prev Res (Phila). 2011 Jul 12. PMID:21750208<ref>PMID:21750208</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3oob" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
Line 28: Line 17:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Peptidylprolyl isomerase]]
+
[[Category: Bode AM]]
-
[[Category: Bode, A M]]
+
[[Category: Dong Z]]
-
[[Category: Dong, Z]]
+
[[Category: Jung SK]]
-
[[Category: Jung, S K]]
+
[[Category: Kim D-J]]
-
[[Category: Kim, D J]]
+
[[Category: Shim J-H]]
-
[[Category: Shim, J H]]
+
[[Category: Urusova DV]]
-
[[Category: Urusova, D V]]
+
[[Category: Zykova TA]]
-
[[Category: Zykova, T A]]
+
-
[[Category: Isomerase]]
+
-
[[Category: Phosphorylation-dependent cis/trans isomerase]]
+
-
[[Category: Proteins with pser/pthr-pro motif]]
+
-
[[Category: Ww domain-like peptidyl prolyl isomerase]]
+

Current revision

Structural and functional insights of directly targeting Pin1 by Epigallocatechin-3-gallate

PDB ID 3oob

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools